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High doses of immunoglobulin G attenuate immune aggregate-mediated
complement activation by enhancing physiologic cleavage of C3b in C3bn- IgG
complexes
HU Lutz, P Stammler, E Jelezarova, M Nater and PJ Spath
Laboratory for Biochemistry, Swiss Federal Institute of Technology, ETH-
Zentrum, Zurich, Switzerland.
Intravenously applied human IgG has beneficial effects in treating
inflammatory diseases, presumably because it has a complement attenuating
role. This role of IgG was studied in vitro by following C3 activation and
inactivation in sera that were supplemented with exogenous human IgG and
incubated with immune aggregates. IgG added at 2 to 10 mg/mL stimulated the
physiologic inactivation of C3b-containing complexes twofold to threefold
in 20% sera. This, in turn, lowered the overall C3 activation by 28%, as
new C3 convertases primarily assembled on C3b-containing complexes.
Exogenous IgG (5 mg/mL) also stimulated inactivation of purified C3b2-IgG
complexes, whereby their half-life dropped from 3-4 to 1.5 minutes in 20%
serum. IgG appeared to act like a modulator of factor H and I because it
did not stimulate inactivation of C3b-containing complexes in factor
I-deficient serum. Thus, the known partial protection of C3bn-IgG complexes
from inactivation by factor H and I was downregulated by high
concentrations of IgG. The ability of high doses of IgG to stimulate
complement inactivation is a novel regulatory role of IgG. This may be one
of the molecular principles for its therapeutic efficacy in treating
complement-mediated inflammations.
Volume 88,
Issue 1,
pp. 184-193,
07/01/1996
Copyright © 1996 by The American Society of Hematology
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